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RBGP1_MOUSE
ID   RBGP1_MOUSE             Reviewed;        1064 AA.
AC   A2AWA9; Q5DTN1; Q8BQ32; Q8C8W3; Q8CD74; Q8R312;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Rab GTPase-activating protein 1;
DE   AltName: Full=GAP and centrosome-associated protein;
DE   AltName: Full=Rab6 GTPase-activating protein GAPCenA;
GN   Name=Rabgap1 {ECO:0000312|MGI:MGI:2385139};
GN   Synonyms=Kiaa4104 {ECO:0000312|EMBL:BAD90509.1};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC31880.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 646-1064 (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC31880.1};
RC   TISSUE=Embryonic spinal ganglion {ECO:0000312|EMBL:BAC34703.1},
RC   Embryonic testis {ECO:0000312|EMBL:BAC27344.1}, and
RC   Retina {ECO:0000312|EMBL:BAC31880.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAD90509.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain {ECO:0000312|EMBL:BAD90509.1};
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:AAH26862.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 733-1064 (ISOFORM 1).
RC   STRAIN=Czech II {ECO:0000312|EMBL:AAH26862.1}, and
RC   FVB/N {ECO:0000312|EMBL:AAH31714.1};
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH31714.1}, and
RC   Mammary tumor {ECO:0000312|EMBL:AAH26862.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-355 AND THR-991, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: May act as a GTPase-activating protein of RAB6A. May play a
CC       role in microtubule nucleation by centrosome. May participate in a
CC       RAB6A-mediated pathway involved in the metaphase-anaphase transition
CC       (By similarity). {ECO:0000250|UniProtKB:Q9Y3P9}.
CC   -!- SUBUNIT: Interacts with RAB6A and tubulin gamma.
CC       {ECO:0000250|UniProtKB:Q9Y3P9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9Y3P9}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y3P9}.
CC       Note=Predominantly cytosolic but also associated with the centrosome.
CC       {ECO:0000250|UniProtKB:Q9Y3P9}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1 {ECO:0000269|Ref.2};
CC         IsoId=A2AWA9-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:16141072};
CC         IsoId=A2AWA9-2; Sequence=VSP_052520, VSP_052521;
CC       Name=3 {ECO:0000269|PubMed:16141072};
CC         IsoId=A2AWA9-3; Sequence=VSP_052516, VSP_052517, VSP_052518,
CC                                  VSP_052519;
CC   -!- DOMAIN: The arginine and glutamine fingers are critical for the GTPase-
CC       activating mechanism, they pull out Rab's 'switch 2' glutamine and
CC       insert in Rab's active site. {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH31714.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC34703.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD90509.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK031315; BAC27344.1; -; mRNA.
DR   EMBL; AK044346; BAC31880.1; -; mRNA.
DR   EMBL; AK051644; BAC34703.1; ALT_INIT; mRNA.
DR   EMBL; AK220489; BAD90509.1; ALT_INIT; mRNA.
DR   EMBL; AL953890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026862; AAH26862.1; ALT_INIT; mRNA.
DR   EMBL; BC031714; AAH31714.1; ALT_INIT; mRNA.
DR   CCDS; CCDS16002.1; -. [A2AWA9-1]
DR   CCDS; CCDS16003.1; -. [A2AWA9-2]
DR   RefSeq; NP_001029132.1; NM_001033960.1. [A2AWA9-2]
DR   RefSeq; NP_666233.2; NM_146121.2. [A2AWA9-1]
DR   RefSeq; XP_006498057.1; XM_006497994.3.
DR   RefSeq; XP_017172964.1; XM_017317475.1.
DR   AlphaFoldDB; A2AWA9; -.
DR   SMR; A2AWA9; -.
DR   BioGRID; 230687; 6.
DR   IntAct; A2AWA9; 1.
DR   STRING; 10090.ENSMUSP00000068835; -.
DR   iPTMnet; A2AWA9; -.
DR   PhosphoSitePlus; A2AWA9; -.
DR   EPD; A2AWA9; -.
DR   MaxQB; A2AWA9; -.
DR   PaxDb; A2AWA9; -.
DR   PeptideAtlas; A2AWA9; -.
DR   PRIDE; A2AWA9; -.
DR   ProteomicsDB; 300311; -. [A2AWA9-1]
DR   ProteomicsDB; 300312; -. [A2AWA9-2]
DR   ProteomicsDB; 300313; -. [A2AWA9-3]
DR   Antibodypedia; 30396; 264 antibodies from 27 providers.
DR   DNASU; 227800; -.
DR   Ensembl; ENSMUST00000061179; ENSMUSP00000061624; ENSMUSG00000035437. [A2AWA9-1]
DR   Ensembl; ENSMUST00000066055; ENSMUSP00000068835; ENSMUSG00000035437. [A2AWA9-2]
DR   Ensembl; ENSMUST00000112920; ENSMUSP00000108542; ENSMUSG00000035437. [A2AWA9-1]
DR   GeneID; 227800; -.
DR   KEGG; mmu:227800; -.
DR   UCSC; uc008jmw.1; mouse. [A2AWA9-3]
DR   UCSC; uc008jmx.1; mouse. [A2AWA9-1]
DR   UCSC; uc008jmy.1; mouse. [A2AWA9-2]
DR   CTD; 23637; -.
DR   MGI; MGI:2385139; Rabgap1.
DR   VEuPathDB; HostDB:ENSMUSG00000035437; -.
DR   eggNOG; KOG1102; Eukaryota.
DR   GeneTree; ENSGT00940000157216; -.
DR   HOGENOM; CLU_007394_0_0_1; -.
DR   InParanoid; A2AWA9; -.
DR   OMA; KPSQGDC; -.
DR   PhylomeDB; A2AWA9; -.
DR   TreeFam; TF317184; -.
DR   BRENDA; 2.3.1.23; 3474.
DR   Reactome; R-MMU-8854214; TBC/RABGAPs.
DR   BioGRID-ORCS; 227800; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Rabgap1; mouse.
DR   PRO; PR:A2AWA9; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; A2AWA9; protein.
DR   Bgee; ENSMUSG00000035437; Expressed in undifferentiated genital tubercle and 245 other tissues.
DR   ExpressionAtlas; A2AWA9; baseline and differential.
DR   Genevisible; A2AWA9; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR   GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISO:MGI.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR   InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR   InterPro; IPR033185; RabGAP1.
DR   PANTHER; PTHR22957:SF439; PTHR22957:SF439; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00566; RabGAP-TBC; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; SSF47923; 2.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW   GTPase activation; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1064
FT                   /note="Rab GTPase-activating protein 1"
FT                   /id="PRO_0000298780"
FT   DOMAIN          137..293
FT                   /note="PID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT   DOMAIN          561..747
FT                   /note="Rab-GAP TBC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          805..1038
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        9..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            603
FT                   /note="Arginine finger"
FT                   /evidence="ECO:0000250"
FT   SITE            644
FT                   /note="Glutamine finger"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         991
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..18
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052516"
FT   VAR_SEQ         19..30
FT                   /note="TLNSEDFVLVSR -> MGLSSLSANKPW (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052517"
FT   VAR_SEQ         363..384
FT                   /note="ESMGKSSDGKSYVITGSWNPKS -> VRFCCCCCCGLFWLWLVFIRNL (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052518"
FT   VAR_SEQ         385..1064
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052519"
FT   VAR_SEQ         804..809
FT                   /note="ISQKKL -> VQQRLL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052520"
FT   VAR_SEQ         810..1064
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_052521"
FT   CONFLICT        646
FT                   /note="Q -> E (in Ref. 1; BAC34703)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1064 AA;  120798 MW;  8AFAB7C7827F0040 CRC64;
     MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK IVGNGSEQQL
     QKELADVLMD PPMDDQPGER SQLDGEGDGP LSNQLSASST INPVPLVGLP KPEMSLPVKP
     GQGDSEVSSP FTPVADEDSV VFNKLTYLGC ASVNAPRSEV EALRMMSILR SQCQISLDVT
     LSVPNVSEGT VRLLDPQTNT EIANYPIYKI LFCVRGHDGT PESDCFAFTE SHYNAELFRI
     HVFRCEIQEA VSRILYSFAT AFRRSAKQTP LSATAAPQTP DSDIFTFSVS LEIKEDDGKG
     YFSAVPKDKD RQCFKLRQGI DKKIVICVQQ TANKELAIER CFGLLLSPGK DVRNSDMHLL
     DLESMGKSSD GKSYVITGSW NPKSPHFQVV NEETPKDKVL FMTTAVDLVI TEVQEPVRFL
     LETKVRVCSP NERLFWPFSK RSTTENFFLK LKQIKQKEKK NNADTLYEVV CLESESERER
     RKTTASPSVR LPQSGSQSSM IPSPPEDDEE EDNDEPLLSG FGDVSKECAE KILETWGELL
     SKWHLNLSVR PKQLSSLVRS GVPEALRGEV WQLLAGCHNN DHLVEKYRIL ITKESPQDSA
     ITRDINRTFP AHDYFKDTGG DGQDSLYKIC KAYSVYDEEI GYCQGQSFLA AVLLLHMPEE
     QAFSVLVKIM FDYGLRELFK QNFEDLHCKF YQLERLMQEY IPDLYNHFLD ISLEAHMYAS
     QWFLTLFTAK FPLYMVFHII DLLLCEGISV IFNVALGLLK TSKDDLLLTD FEGALKFFRV
     QLPKRYRSEE NAKRLMELAC NTKISQKKLK KFEKEYHTMR EQQAQQEDPI ERFERENRRL
     QEANMRLEQE NDDLAHELVT SKIALRKDLD NAEEKADALN KELLMTKQKL IDAEDEKRRL
     EEESAQLKEM CRRELDKAES EIKKNSSIIG DYKQICSQLS ERLEKQQTAN KVEIEKIRQK
     VDDCDRCRDF FNKEGRVKGI SSAKGVSDED TDEEKETLKN QLREMELELA QTKLQLVEAE
     CKIQDLEHHL GLALSEVQAA KKTWFNRTLS SIKTATGVQG KETC
 
 
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